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Database: UniProt
Entry: K7SFD9_GLUOY
LinkDB: K7SFD9_GLUOY
Original site: K7SFD9_GLUOY 
ID   K7SFD9_GLUOY            Unreviewed;       452 AA.
AC   K7SFD9;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-SEP-2017, entry version 35.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=B932_2532 {ECO:0000313|EMBL:AFW02084.1};
OS   Gluconobacter oxydans H24.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1224746 {ECO:0000313|EMBL:AFW02084.1, ECO:0000313|Proteomes:UP000000223};
RN   [1] {ECO:0000313|EMBL:AFW02084.1, ECO:0000313|Proteomes:UP000000223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H24 {ECO:0000313|EMBL:AFW02084.1};
RX   PubMed=23472221;
RA   Ge X., Zhao Y., Hou W., Zhang W., Chen W., Wang J., Zhao N., Lin J.,
RA   Wang W., Chen M., Wang Q., Jiao Y., Yuan Z., Xiong X.;
RT   "Complete Genome Sequence of the Industrial Strain Gluconobacter
RT   oxydans H24.";
RL   Genome Announc. 1:E00003-E00013(2013).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
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DR   EMBL; CP003926; AFW02084.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFW02084; AFW02084; B932_2532.
DR   KEGG; goh:B932_2532; -.
DR   PATRIC; fig|1224746.3.peg.2489; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000223; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000223};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000223}.
FT   DOMAIN      150    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   452 AA;  51098 MW;  5145318E8AFFF7B1 CRC64;
     MEASWHKVRE KLKGEVGEVE YRTWLRQIVL GPIEDGELIL YLPTRFLRDW VRSQYEERLQ
     TLWRTERADV QGIELQVKRG LPEVPPSADI ESDSAVEEVA AQVAVSHEVR SDLAVPLDPR
     FSFDSFVVGK PNEFAYACAR RVAEKPSSPG FNPLFLYGGV GLGKTHLMHA IGSELTKTGN
     VSVAYMSAEK FMYRFIAAIR SQSTMEFKEQ LRSVDVLMID DLQFLIGKDN TQEEFFHTFN
     ALVDAGRQII VSADKSPSDL SGLEDRLRTR LGCGMVADIH ATTFELRISI LEAKAKASGT
     HVPSKVLEYL AHKITTNVRE LEGALNRLIA HADLVGRPVT LDTTQDVLKD MLKAHDRRVT
     IEEIQRKVAE HWNIRLTDMS SARRARAVAR PRQVAMFLAK QLTSRSLPEI GRKFGNRDHT
     TVMHAVNRVA ELMEQDTSFA EDVELMRRML EG
//
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